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dc.contributor.authorPunet, Xavier
dc.contributor.authorMauchauffé, Rodolphe
dc.contributor.authorGiannotti, Marina I.
dc.contributor.authorRodriguez Cabello, Jose Carlos
dc.contributor.authorSanz Carrasco, Fausto
dc.contributor.authorEngel López, Elisabeth
dc.contributor.authorMateos Timoneda, Miguel Ángel
dc.contributor.authorPlanell Estany, Josep Anton
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament de Ciència dels Materials i Enginyeria Metal·lúrgica
dc.contributor.otherInstitut de Bioenginyeria de Catalunya
dc.date.accessioned2013-11-15T12:39:20Z
dc.date.created2013-08
dc.date.issued2013-08
dc.identifier.citationPunet, X. [et al.]. Enhanced cell-material interactions through the biofunctionalization of polymeric surfaces with engineered peptides. "Biomacromolecules", Agost 2013, vol. 14, núm. 8, p. 2690-2702.
dc.identifier.issn1525-7797
dc.identifier.urihttp://hdl.handle.net/2117/20625
dc.description.abstractResearch on surface modi fi cation of polymeric materials to guide the cellular activity in biomaterials designed for tissue engineering applications has mostly focused on the use of natural extracellular matrix (ECM) proteins and short peptides, such as RGD. However, the use of engineered proteins can gather the advantages of these strategies and avoid the main drawbacks. In this study, recombinant engineered proteins called elastin- like recombinamers (ELRs) have been used to functionalize poly(lactic) acid (PLA) model surfaces. The structure of the ELRs has been designed to include the integrin ligand RGDS and the cross-linking module VPGKG. Surface functionalization has been characterized and optimized by means of ELISA and atomic force microscopy (AFM). The results suggest that ELR functionalization creates a nonfouling canvas able to restrict unspeci fi c adsorption of proteins. Moreover, AFM analysis reveals the conformation and disposition of ELRs on the surface. Biological performance of PLA surfaces functionalized with ELRs has been studied and compared with the use of short peptides. Cell response has been assessed for di ff erent functionalization conditions in the presence and absence of the bovine serum albumin (BSA) protein, which could interfere with the surface − cell interaction by adsorbing on the interface. Studies have shown that ELRs are able to elicit higher rates of cell attachment, stronger cell anchorages and faster levels of proliferation than peptides. This work has demonstrated that the use of engineered proteins is a more e ffi cient strategy to guide the cellular activity than the use of short peptides, because they not only allow for better cell attachment and proliferation, but also can provide more complex properties such as the creation of nonfouling surfaces
dc.format.extent13 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria dels materials
dc.subject.lcshBiomechanics
dc.subject.otherAdsorption of proteins
dc.subject.otherBiofunctionalization
dc.subject.otherBiological performance
dc.subject.otherBovine serum albumin proteins (BSA)
dc.subject.otherCell-material interaction
dc.subject.otherExtracellular matrix protein
dc.subject.otherSurface Functionalization
dc.subject.otherTissue engineering applications
dc.titleEnhanced cell-material interactions through the biofunctionalization of polymeric surfaces with engineered peptides
dc.typeArticle
dc.subject.lemacBiomecànica
dc.subject.lemacEnginyeria de teixits
dc.contributor.groupUniversitat Politècnica de Catalunya. BBT - Biomaterials, Biomecànica i Enginyeria de Teixits
dc.identifier.doi10.1021/bm4005436
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://pubs.acs.org/doi/pdf/10.1021/bm4005436
dc.rights.accessRestricted access - publisher's policy
local.identifier.drac12773680
dc.description.versionPostprint (published version)
dc.date.lift10000-01-01
dc.contributor.covenanteeUniversidad de Valladolid
local.citation.authorPunet, X.; Mauchauffé, R.; Giannotti, M.I.; Rodriguez-Cabello , J.C.; Sanz, Fausto; Engel, E.; Mateos-Timoneda, M.A.; Planell, J.
local.citation.publicationNameBiomacromolecules
local.citation.volume14
local.citation.number8
local.citation.startingPage2690
local.citation.endingPage2702


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Attribution-NonCommercial-NoDerivs 3.0 Spain
Except where otherwise noted, content on this work is licensed under a Creative Commons license : Attribution-NonCommercial-NoDerivs 3.0 Spain